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Information on EC 4.3.2.2 - adenylosuccinate lyase and Organism(s) Pyrobaculum aerophilum and UniProt Accession Q8ZY28

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.2 adenylosuccinate lyase
IUBMB Comments
Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
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This record set is specific for:
Pyrobaculum aerophilum
UNIPROT: Q8ZY28
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Word Map
The taxonomic range for the selected organisms is: Pyrobaculum aerophilum
The enzyme appears in selected viruses and cellular organisms
Synonyms
adenylosuccinate lyase, asase, adenylosuccinase, succino-amp lyase, amps lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylosuccinase
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-
-
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adenylosuccinate lyase
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AMPS lyase
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-
-
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ASASE
-
-
-
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ASL
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-
-
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Glutamyl-tRNA synthetase regulatory factor
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-
-
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lyase, adenylosuccinate
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-
-
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succino AMP-lyase
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-
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succino-AMP lyase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
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-
SYSTEMATIC NAME
IUBMB Comments
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-81-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
show the reaction diagram
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
show the reaction diagram
-
-
-
-
?
adenylosuccinate
AMP + fumarate
show the reaction diagram
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
show the reaction diagram
-
-
-
-
?
adenylosuccinate
AMP + fumarate
show the reaction diagram
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trans-4-hydroxy-2-nonenal
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10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
monomer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure is determined to 2.1 resolution. Hanging drop vapor diffusion method at 18°C
at a resolution of 2.1 A
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the structure of adenylosuccinate lyase reveals that this protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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participates in the purine biosynthetic pathway, enzyme defects result in psychomotor retardation, epilepsy, muscle wasting and autistic features
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crifo, C.; Siems, W.; Soro, S.; Salerno, C.
Inhibition of defective adenylosuccinate lyase by HNE: a neurological disease that may be affected by oxidative stress
Biofactors
24
131-136
2005
Bacillus subtilis, Homo sapiens, Pyrobaculum aerophilum, Thermotoga maritima
Manually annotated by BRENDA team
Spiegel, E.K.; Colman, R.F.; Patterson, D.
Adenylosuccinate lyase deficiency
Mol. Genet. Metab.
89
19-31
2006
Bacillus subtilis, Homo sapiens, Mus musculus, Pyrobaculum aerophilum, Thermotoga maritima (Q9X0I0)
Manually annotated by BRENDA team
Toth, E.A.; Worby, C.; Dixon, J.E.; Goedken, E.R.; Marqusee, S.; Yeates, T.O.
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
J. Mol. Biol.
301
433-450
2000
Pyrobaculum aerophilum (Q8ZY28), Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523 (Q8ZY28)
Manually annotated by BRENDA team